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Literature summary extracted from

  • Mijatovic, S.; Gadda, G.
    Oxidation of alkyl nitronates catalyzed by 2-nitropropane dioxygenase from Hansenula mrakii (2008), Arch. Biochem. Biophys., 473, 61-68.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.13.12.16 expressed in Escherichia coli Cyberlindnera mrakii

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.13.12.16 additional information superoxide dismutase and catalase have no effect on the enzymatic activity Cyberlindnera mrakii

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.13.12.16 additional information the enzyme contains negligible amounts of iron, manganese, zinc, and copper ions, which are not catalytically relevant Cyberlindnera mrakii

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.13.12.16 40000
-
 SDS-PAGE Cyberlindnera mrakii

Organism

EC Number Organism UniProt Comment Textmining
1.13.12.16 Cyberlindnera mrakii Q12723
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.13.12.16
-
 Cyberlindnera mrakii

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.13.12.16 butyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + butanal
-
 ?
1.13.12.16 ethylnitronate + O2
-
 Cyberlindnera mrakii NO2- + acetaldehyde
-
 ?
1.13.12.16 hexyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + hexanal
-
 ?
1.13.12.16 additional information anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicated that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes Cyberlindnera mrakii ?
-
 ?
1.13.12.16 additional information anaerobic substrate reduction and kinetic data using a Clark oxygen electrode to measure rates of oxygen consumption indicates that the enzyme is active on a broad range of alkyl nitronates, with a marked preference for unbranched substrates over propyl-2-nitronate. The enzyme utilizes alkyl nitronates for catalysis, but not nitroalkanes Cyberlindnera mrakii ?
-
 ?
1.13.12.16 pentyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + pentanal
-
 ?
1.13.12.16 propyl-1-nitronate + O2
-
 Cyberlindnera mrakii NO2- + propionaldehyde
-
 ?
1.13.12.16 propyl-2-nitronate + O2
-
 Cyberlindnera mrakii NO2- + acetone
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.13.12.16 2-nitropropane dioxygenase
-
 Cyberlindnera mrakii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.13.12.16 30
-
 assay at Cyberlindnera mrakii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.13.12.16 7.4
-
 assay at Cyberlindnera mrakii
1.13.12.16 8
-
 assay at Cyberlindnera mrakii

Cofactor

EC Number Cofactor Comment Organism Structure
1.13.12.16 FMN present in a 1:1 stoichiometry with the protein. The tight binding of sulfite (Kd = 0.09 mM, at pH 8 and 15°C) to the enzyme and the formation of the anionic flavosemiquinone upon anaerobic incubation with alkyl nitronates are consistent with the presence of a positively charged group in proximity of the N(1)-C(2)=O atoms of the FMN cofactor Cyberlindnera mrakii

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.13.12.16 1.6
-
 propyl-2-nitronate
-
 Cyberlindnera mrakii
1.13.12.16 112
-
 butyl-1-nitronate
-
 Cyberlindnera mrakii
1.13.12.16 121
-
 pentyl-1-nitronate
-
 Cyberlindnera mrakii
1.13.12.16 129
-
 ethylnitronate
-
 Cyberlindnera mrakii
1.13.12.16 130
-
 hexyl-1-nitronate
-
 Cyberlindnera mrakii
1.13.12.16 170
-
 propyl-1-nitronate
-
 Cyberlindnera mrakii